Structure of PDB 1pl0 Chain B

Receptor sequence
>1pl0B (length=587) Species: 9606 (Homo sapiens) [Search protein sequence]
GQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSE
LTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNL
YPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVV
VSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQ
MPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKEL
KEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAY
ARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTI
LSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNV
VTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIH
CTRLAGDKANYWWLRHHPQVLSMKFKTGVAEISNAIDQYVTGTIGEDEDL
IKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSG
VAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
3D structure
PDB1pl0 Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-carboxamide Ribonucleotide Transformylase/IMP Cyclohydrolase in Complex with Potent Sulfonyl-containing Antifolates.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K266 H267 N431 H592
Catalytic site (residue number reindexed from 1) K263 H264 N428 H587
Enzyme Commision number 2.1.2.3: phosphoribosylaminoimidazolecarboxamide formyltransferase.
3.5.4.10: IMP cyclohydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AMZ B R451 A540 F541 R588 F590 R448 A535 F536 R583 F585
BS02 BW2 B S450 R451 I452 F541 P543 F544 N547 S447 R448 I449 F536 P538 F539 N542 PDBbind-CN: -logKd/Ki=8.22,Ki=6nM
BindingDB: Ki=6.0nM,IC50=1000nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003937 IMP cyclohydrolase activity
GO:0004643 phosphoribosylaminoimidazolecarboxamide formyltransferase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity
GO:0045296 cadherin binding
Biological Process
GO:0003360 brainstem development
GO:0006139 nucleobase-containing compound metabolic process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0021549 cerebellum development
GO:0021987 cerebral cortex development
GO:0031100 animal organ regeneration
GO:0044208 'de novo' AMP biosynthetic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0097294 'de novo' XMP biosynthetic process
GO:0098761 cellular response to interleukin-7
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pl0, PDBe:1pl0, PDBj:1pl0
PDBsum1pl0
PubMed14966129
UniProtP31939|PUR9_HUMAN Bifunctional purine biosynthesis protein ATIC (Gene Name=ATIC)

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